7nlv

WILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE II

Method: X-RAY DIFFRACTION Dmax: 64.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Streptavidin

Streptomyces avidinii

UniProt P22629

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain AAA; UniProt 37–163 Chain BBB; UniProt 37–163 Chain CCC; UniProt 37–163 Chain DDD; UniProt 37–163 Not recorded UJE 5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)-N-((S)-pyrrolidin-3-yl)pentanamide × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25 mg/mL protein in deionised water is mixed at equal volume with 52% MPD. Resolution 1.29 Å R-free 0.247

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

312 other PDB entries and 368 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAV_STRAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 2–128; UniProt 37–163 Author chain BBB; PDBConstruct 2–128; UniProt 37–163 Author chain CCC; PDBConstruct 2–128; UniProt 37–163 Author chain DDD; PDBConstruct 2–128; UniProt 37–163

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7nlv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nlv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7nlv
Deposition date deposition_date2021-02-22
Structure title titleWILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE II
Keywords keywordsBiotin-binding protein, streptavidin, artificial enzyme, beta-barrel, DE NOVO PROTEIN; DE NOVO PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.23
Radius of gyration Rg (electron density) rg_electron21.14
Forward intensity I(0) i046418700.00
Molecular weight molecular_weight51139.0 kDa
Excluded volume excluded_volume63110 ų
Envelope volume envelope_volume72018 ų
Hydration-shell volume shell_volume27097 ų
Envelope diameter envelope_diameter66.5
Shell Rg shell_rg28.83
Envelope Rg envelope_rg21.47
Shape Rg shape_rg21.12
Total Rg total_rg22.07
Total atoms total_atoms3621
Residues n_residues473
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax64.4
Rg (real space) rg_real22.07
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real4.6420e+07
I(0) uncertainty (real space) i0_real_error5.8510e+05
Rg (reciprocal space) rg_reciprocal22.11
I(0) (reciprocal space) i0_reciprocal46420000.0000
Solution quality estimate total_estimate0.8357
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.087
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15200000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)